RegulonDB RegulonDB 10.8: Gene Form
   

tyrB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

tyrB alr yjbS TyrR TyrR TSS_4891 TSS_4891 TSS_4890 TSS_4890 tyrBp tyrBp

Gene      
Name: tyrB    Texpresso search in the literature
Synonym(s): ECK4046, EG11040, b4054
Genome position(nucleotides): 4267114 --> 4268307 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
52.76
External database links:  
ASAP:
ABE-0013278
CGSC:
57
ECHOBASE:
EB1033
OU-MICROARRAY:
b4054
PortEco:
tyrB
STRING:
511145.b4054
COLOMBOS: tyrB


Shine dalgarno      
Sequence: ccgtaaacctGGAGAAccatcgcGTG


Product      
Name: tyrosine aminotransferase
Synonym(s): TyrB
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 43.538
Isoelectric point: 5.143
Motif(s):
 
Type Positions Sequence
27 -> 392 DKVNLSIGLYYNEDGIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRFNDLLATLKTLPARSIVLLHPCCHNPTGADLTNDQWDAVIEILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLNDEALKASWLAEVEEMRTRILAMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVDRLREEFGVYLIASGRMCVAGLNTANVQRVAKA

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.13 - phenylalanine
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.14 - tyrosine
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.19 - leucine
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0003824 - catalytic activity
GO:0016740 - transferase activity
GO:0008483 - transaminase activity
GO:0008793 - aromatic-amino-acid:2-oxoglutarate aminotransferase activity
GO:0004838 - L-tyrosine:2-oxoglutarate aminotransferase activity
GO:0050048 - L-leucine:2-oxoglutarate aminotransferase activity
GO:0030170 - pyridoxal phosphate binding
GO:0004084 - branched-chain-amino-acid transaminase activity
GO:0042802 - identical protein binding
GO:0042803 - protein homodimerization activity
GO:0080130 - L-phenylalanine:2-oxoglutarate aminotransferase activity
biological_process GO:0006520 - cellular amino acid metabolic process
GO:0006532 - aspartate biosynthetic process
GO:0006571 - tyrosine biosynthetic process
GO:0008652 - cellular amino acid biosynthetic process
GO:0009058 - biosynthetic process
GO:0009073 - aromatic amino acid family biosynthetic process
GO:0009094 - L-phenylalanine biosynthetic process
GO:0009098 - leucine biosynthetic process
GO:0019292 - tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
GO:0033585 - L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Reference(s): [1] Fotheringham IG., et al., 1986
[2] Gelfand DH., et al., 1977
[3] Kuramitsu S., et al., 1985
External database links:  
ECOCYC:
TYRB-MONOMER
ECOLIWIKI:
b4054
INTERPRO:
IPR004838
INTERPRO:
IPR015424
INTERPRO:
IPR015422
INTERPRO:
IPR015421
INTERPRO:
IPR004839
INTERPRO:
IPR000796
MODBASE:
P04693
PANTHER:
PTHR11879
PDB:
3FSL
PDB:
3TAT
PFAM:
PF00155
PRIDE:
P04693
PRINTS:
PR00799
PRODB:
PRO_000024151
PROSITE:
PS00105
REFSEQ:
NP_418478
SMR:
P04693
UNIPROT:
P04693


Operon      
Name: tyrB         
Operon arrangement:
Transcription unit        Promoter
tyrB


Transcriptional Regulation      
Display Regulation             
Repressed by: TyrR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_4890 4267202 forward nd [RS-EPT-CBR] [4]
  promoter TSS_4891 4267210 forward nd [RS-EPT-CBR] [4]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Fotheringham IG., Dacey SA., Taylor PP., Smith TJ., Hunter MG., Finlay ME., Primrose SB., Parker DM., Edwards RM., 1986, The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes., Biochem J 234(3):593-604

 [2] Gelfand DH., Rudo N., 1977, Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC., J Bacteriol 130(1):441-4

 [3] Kuramitsu S., Inoue K., Ogawa T., Ogawa H., Kagamiyama H., 1985, Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene., Biochem Biophys Res Commun 133(1):134-9

 [4] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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